EP0351950A2 - Verwendung von Plasma zur Immobilisierung von Proteinen auf Polymeroberflächen - Google Patents

Verwendung von Plasma zur Immobilisierung von Proteinen auf Polymeroberflächen Download PDF

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Publication number
EP0351950A2
EP0351950A2 EP89305776A EP89305776A EP0351950A2 EP 0351950 A2 EP0351950 A2 EP 0351950A2 EP 89305776 A EP89305776 A EP 89305776A EP 89305776 A EP89305776 A EP 89305776A EP 0351950 A2 EP0351950 A2 EP 0351950A2
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EP
European Patent Office
Prior art keywords
protein
polymer
membrane
plasma
buffer
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Withdrawn
Application number
EP89305776A
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English (en)
French (fr)
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EP0351950A3 (de
Inventor
Tien-Tsai Hsu
Mann-Tchao No.4 Professor Residential Distr. Wang
Kuang-Pin Hsiung
Ging Ho Hsiue
Min-Shyan Sheu
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Industrial Technology Research Institute ITRI
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Industrial Technology Research Institute ITRI
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Publication of EP0351950A2 publication Critical patent/EP0351950A2/de
Publication of EP0351950A3 publication Critical patent/EP0351950A3/de
Withdrawn legal-status Critical Current

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/001—Enzyme electrodes
    • C12Q1/002—Electrode membranes
    • C12Q1/003—Functionalisation
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
    • C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
    • C12N11/08—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer
    • C12N11/082—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/544—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals the carrier being organic
    • G01N33/545—Synthetic resin

Definitions

  • the subject invention relates to the use of a plasma activation method to induce protein immobilization on a polymeric matrix.
  • a plasma activation method to induce protein immobilization on a polymeric matrix.
  • protein immobilization methods which are available to immobilize protein on different kinds of materials, for example, chemical activation, entrapment and crosslinking.
  • These conventional methods suffer from many shortcomings such as forming products of low stability and low activity and the inability of any one method to work well with a variety of proteins.
  • the instant invention relates to a plasma activation method which can be used to immobilize a wide range of proteins on the polymeric matrix by using substantially one and the same technique.
  • a protein mixture is first prepared with or without a crosslinking agent and then applied to a membrane.
  • the treated membrane is placed into the reaction chamber which acts as a plasma generator and a vacuum drier.
  • the plasma is generated in a nitrogen, oxygen or ammonia environment under the desired conditions of pressure and temperature, for a defined period of time, to properly activate the protein and membrane molecules without damaging the normal configuration of the protein molecules.
  • the covalent bonds formed among protein molecules and protein-membrane molecules anchor the protein to the surface of the membrane and stabilize the protein configuration.
  • the membrane is removed from the reaction chamber and washed with a buffer solution to remove the unbound protein.
  • the treated membranes may be stored in the buffer solution for later use or used directly.
  • a protein membrane having good activity and stability can be produced. It may be used for many biotechnological and biomedical applications, for example, as a membrane reactor in biotransformation process, as an enzyme membrane in biosensing instruments, and as an antigen-antibody membrane in immunoassays.
  • the novel plasma activation method can be used to immobilize the protein on the polymeric matrix regardless of the form of the latter's surfaces. Accordingly, the present invention may be used to form myriad biosensors and many types of protein matrices in large or small quantities, including the large scale production of protein membranes.
  • the use of the process for immobilizing glucose oxidase, lactate oxidase, 1-glutamate decarboxylase, 1-lysine decarboxylase and invertase, mutarotase, and glucose oxidase mixtures for the biosensing instrument purpose has already been established.
  • proteins may be immobilized in accordance with the instant invention.
  • these include, for example, glucose oxidase, 1-glutamate decarboxylase, 1-lysine decarboxylase, urease, uricase, insulin monoclonal antibody, phenol oxidase, alkaline phosphatase, invertase and mutarotase.
  • Polymeric materials which may be used to immobilize the proteins include polyolefins such as hydrophobic and hydrophilic polyethylene and polypropylene and cellulose acetate, e.g., cuprophane film. Hydrophilic polypropylene membranes are most preferred. It will be understood, however, that many plastics, elastomers, and fibers having similarly reactive surfaces may be treated with the protein under appropriate reaction conditions.
  • the particular surface configuration of the polymeric material may vary widely, depending on the desired application. Most preferably a membrane type surface is employed, though beads, plates and tubes may conveniently be used.
  • a typical plasma generator is the radio frequency (13.56 MHz) generator PE-II Plasma System made by Technics Co.
  • the temperature during the plasma generation may range from 0° to 40°C, preferably from 0° to 25°C.
  • the pressure may range from 0.1 to 0.4 torr, preferably from 0.1 to 0.2 torr.
  • the power applied to the plasma generator will generally range from 25 to 300 watts, preferably from 50 to 300 watts.
  • the time necessary for activation ranges from 1 to 10 minutes, preferably from 3 to 5 minutes.
  • the plasma activation may take place in the presence of crosslinking agents such as glutaraldehyde.
  • crosslinking agents such as glutaraldehyde.
  • the preferred agent and optimum amount used may be readily determined by those skilled in the art.
  • the treated product is rinsed in a buffer solution to remove unbound protein.
  • buffer solutions may be employed for this washing step, as well as for storage.
  • buffers include phosphate buffers, tris buffers and citric buffers. The concentration used may be readily determined and is dependent on the protein employed.
  • the immobilized protein may be used in biotransformation or biosensing instruments, as well as for immunoassays.
  • immobilized tyrosinase may be used in the bioconversion of tyrosine to 1-DOPA and insulin monoclonal antibody can be used to assay the insulin content in clinical samples.
  • other applications of immobilized protein are well known in biotechnology and protein engineering.
  • a protein solution is first prepared by dissolving the protein in the buffer with or without a crosslinking reagent.
  • the polymeric material is cut into appropriate shapes and dimensions, washed with distilled water or NaOH solution to remove any contamination, and dried.
  • the protein solution is pipetted onto the pretreated membrane and spread evenly with a spatula to form the samples.
  • the plasma apparatus (Technics Co.), shown in Fig. 1, is operated by sequentially turning on the gases (1), the main power (3), the vacuum pump (5) and the water circulation pump (6).
  • the control switch is turned to manual (3) and the plasma power turned on.
  • the vacuum reaches 0.1 torr, plasma forms.
  • the time is set when the plasma is ready for use.
  • the samples are loaded on the lower electrode by setting the control switch to auto (3) and turning on the vent switch to open the reaction chamber (2).
  • the reaction chamber is then closed and the process initiated by pushing the start button (4).
  • the process is then carried out in accordance with the preset conditions.
  • the reaction chamber is vented and the treated membrane samples removed.
  • the treated protein membrane is washed several times with an appropriate buffer for at least 12 hours.
  • the membrane prepared is then stored in a storage solution or used directly.
  • the protein membrane may be analyzed by using a FTIR spectrophotometer, by protein stain or any known protein determination methods. If the protein is an enzyme, then it can be analyzed by detection of the enzyme activity. If the protein is an antibody, then it can be measured by Enzyme Immuno Assay (EIA) or Radio Immuno Assay (RIA).
  • EIA Enzyme Immuno Assay
  • RIA Radio Immuno Assay
  • the term "biosensor” means a device for determining the amount of a given substance. As shown in Fig. 2, it consists of transducer (1), analyzer (2), recorder (3), enzyme membrane (4), reaction chamber (5), stirrer (6) and temperature controller (7).
  • the biosensor employs an enzyme as the receptor it is also called an “enzyme sensor” and, if the enzyme sensor employs an electrochemical device as the transducer portion, then it is called an “enzyme electrode”.
  • Example 1 Glucose enzyme electrode
  • a hydrophilic polypropylene membrane is formed into a ring having an 8 mm inside diameter ("ID").
  • ID 8 mm inside diameter
  • the shaped membrane is washed with 0.1 M sodium chloride and distilled water, dried and stored in a dessicator for later use.
  • glucose oxidase (EC 1.1.3.4) Type X (Sigma Co., USA) is dissolved in 1 ml of 0.1 M potassium phosphate buffer at pH 5.5.
  • bovine serum albumin are dissolved in 1 ml of the same buffer. To complete enzyme solution preparation, the two solutions are mixed together.
  • the transducer (1) is a Clark's oxygen electrode and the analyzer (2) is an oxygen meter.
  • the recorder (3) is Linseis 6512 strip chart recorder. The temperature is set to 30°C (7).
  • the glucose oxidase membrane is held on the electrode surface with a cuprophane membrane and an O-ring.
  • One-half ml of 1.6 g/dl glucose is added to adjust the zero oxygen tension.
  • the chamber (5) is washed and refilled with 4.9 ml buffer to adjust span.
  • 0.1 ml of standard is used to develop the calibration curve.
  • the sample is added and the concentration determined from the calibration curve.
  • Fig. 3 From Fig. 3, it can be seen that the difference between different enzyme membrane prepared with plasma treatment is very small.
  • the optimum pH range is from pH 4.5 to 7.5 (Fig. 4).
  • the buffer concentration ranging from 0.1 M to 0.8 M, has no influence on the glucose oxidase membrane (Fig. 5).
  • the membrane stored in glycerol buffer at 4°C for 45 days, retains 50% of its original activity as shown in Fig.
  • the glucose oxidase membrane prepared as described above can be used not only as an enzyme electrode in the fermentation industry, but also for clinical tests for diabetes and in food processing for sweetness tests. It can also be used for the bioconversion of glucose into glutonic acid.
  • a hydrophilic polypropylene membrane is cut into a 5 mm ID ring.
  • the shaped membrane is washed with 0.1 M sodium chloride and distilled water, dried and stored in a dessicator for later use.
  • glucose oxidase lactate oxidase from Pediococcus species
  • Sigma Co., USA Eight mg of glucose oxidase (lactate oxidase from Pediococcus species) (Sigma Co., USA) is dissolved in 1 ml of 0.1 M potassium phosphate buffer at pH 7.0. Forty mg of bovine serum albumin are dissolved in 1 ml of the same buffer. To complete enzyme solution preparation, the two solutions are mixed together.
  • the transducer is an Able's hydrogen peroxide electrode and the analyzer is a hydrogen peroxide meter.
  • the recorder is Linseis 6512 strip chart recorder. The temperature is set to 30°C.
  • the lactate oxidase membrane is held on the electrode surface with a cuprophane membrane and an O-ring.
  • One-tenth ml of 2.5 g/dl lactic acid is added to adjust the zero hydrogen peroxide tension.
  • the chamber (5) is washed and refilled with 4.9 ml buffer to adjust span.
  • 0.1 ml of standard is used to develop the calibration curve.
  • the sample is added and the concentration determined from the calibration curve.
  • the lactate oxidase membrane prepared in this manner can be applied not only to a lactic acid enzyme electrode for clinical, fermentation and food industries, but also for lactic acid production.
  • a hydrophilic polypropylene membrane is cut into an 11 mm ID ring.
  • the shaped membrane is washed with 0.1 M sodium chloride and distilled water, dried and stored in a dessicator for later use.
  • the transducer is an ORION carbon dioxide electrode and the analyzer is an ORION pH meter.
  • the recorder is Linseis 6512 strip chart recorder. The temperature is set to 30°C.
  • the 1-glutamate decarboxylase membrane is held on the electrode surface with a cuprophane membrane and an O-ring. Four and one-half ml of buffer are added. When equilibrium is achieved, 0.5 ml of standard is used to develop the calibration curve. The sample is added and the concentration determined from the calibration curve.
  • the enzyme electrode prepared by the immobilized glutamate decarboxylase can be used to detect the glutamic acid content in food additives and in fermentation processes.
  • a hydrophilic polypropylene membrane is cut into an 11 mm ID ring.
  • the shaped membrane is washed with 0.1 M sodium chloride and distilled water, dried and stored in a dessicator for later use.
  • the transducer is an ORION carbon dioxide electrode and the analyzer is an ORION pH meter.
  • the recorder is Linseis 6512 strip chart recorder. The temperature is set to 30°C.
  • the 1-lysine decarboxylase membrane is held on the electrode surface with a cuprophane membrane and an O-ring. Four and nine-tenths ml of buffer are added. When equilibrium is achieved, 0.1 ml of standard is used to develop the calibration curve. The sample is added and the concentration determined from the calibration curve.
  • the enzyme electrode prepared by the immobilized lysine decarboxylase can be used to detect the lysine content in food additives and in fermentation processes.
  • a hydrophilic polypropylene membrane is cut into a 5 mm ID ring.
  • the shaped membrane is washed with 0.1 M sodium chloride and distilled water, dried and stored in a dessicator for later use.
  • glucose oxidase 100 mg invertase, 10 mg mutarotase, 20 mg of bovine serum albumin are dissolved in 1 ml of 0.1 M potassium phosphate buffer at pH 6.5.
  • the transducer is an Able's hydrogen peroxide electrode and the analyzer is a hydrogen peroxide meter.
  • the recorder is Linseis 6512 strip chart recorder. The temperature is set to 30°C.
  • sucrose enzyme membrane is held on the electrode surface with a cuprophane membrane and an O-ring.
  • One-tenth ml of 2 g/dl lactic acid is added to adjust the zero hydrogen peroxide tension.
  • Four and nine-tenths ml of buffer are added.
  • 0.1 ml of standard is used to develop the calibration curve. The sample is added and the concentration determined from the calibration curve.
  • the data show that the optimum pH range is from 6.5 to 7.0 (Fig. 18).
  • the buffer concentration range from 0.1 M to 0.3 M has no influence on the sucrose enzyme membrane (Fig. 19).
  • the membrane stored in glycerol buffer at 4°C, has activity for over one month.

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  • Life Sciences & Earth Sciences (AREA)
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  • Urology & Nephrology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Physics & Mathematics (AREA)
  • General Engineering & Computer Science (AREA)
  • Analytical Chemistry (AREA)
  • Food Science & Technology (AREA)
  • Biophysics (AREA)
  • Cell Biology (AREA)
  • Medicinal Chemistry (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
  • Peptides Or Proteins (AREA)
EP89305776A 1988-07-18 1989-06-07 Verwendung von Plasma zur Immobilisierung von Proteinen auf Polymeroberflächen Withdrawn EP0351950A3 (de)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US07/220,570 US5028657A (en) 1988-07-18 1988-07-18 Use of plasma to immobilize protein on polymeric surfaces
US220570 1988-07-18

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EP0351950A2 true EP0351950A2 (de) 1990-01-24
EP0351950A3 EP0351950A3 (de) 1990-03-28

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1995034814A1 (en) * 1994-06-13 1995-12-21 Abbott Laboratories Plasma treatment of polymeric materials to enhance immobilization of analytes thereto
FR2847583A1 (fr) * 2002-11-27 2004-05-28 Centre Nat Rech Scient Procede d'oligomerisation de molecules, dispositif de mise en oeuvre dudit procede et utilisation
US7666478B2 (en) 2004-04-30 2010-02-23 Vlaamse Instelling Voor Technologisch Onderzoek (Vito) Biomolecule immobilisation using atmospheric plasma technology
US20120171354A1 (en) * 2010-12-13 2012-07-05 Enbio Limited Implantable medical devices

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US5750065A (en) * 1993-01-25 1998-05-12 Institute Of Gas Technology Adsorption of PCB's using biosorbents
US5561045A (en) * 1994-01-04 1996-10-01 Intracel Corporation Detection reagent, article, and immunoassay method
JP2000039401A (ja) * 1998-03-24 2000-02-08 Dainippon Printing Co Ltd 表面プラズモン共鳴バイオセンサ―用測定セル及びその製造方法
AU1055001A (en) * 1999-11-04 2001-05-14 Center For Advanced Science And Technology Incubation, Ltd. Method for immobilizing material
TWI223069B (en) * 2000-05-12 2004-11-01 Ind Tech Res Inst Active slide and the preparation method thereof
US7960184B2 (en) * 2002-09-20 2011-06-14 George Mason Intellectual Properties, Inc. Methods and devices for active bioassay
US7276283B2 (en) * 2004-03-24 2007-10-02 Wisconsin Alumni Research Foundation Plasma-enhanced functionalization of carbon-containing substrates
US7723126B2 (en) * 2004-03-24 2010-05-25 Wisconsin Alumni Research Foundation Plasma-enhanced functionalization of inorganic oxide surfaces
US7928076B2 (en) * 2005-12-15 2011-04-19 E. I. Du Pont De Nemours And Company Polypropylene binding peptides and methods of use
EP2004735A4 (de) * 2006-03-15 2014-03-12 Univ Sydney Aktivierte polymere, die biologische moleküle binden
US8029902B2 (en) * 2006-12-11 2011-10-04 Wisconsin Alumni Research Foundation Plasma-enhanced functionalization of substrate surfaces with quaternary ammonium and quaternary phosphonium groups

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EP0104608A1 (de) * 1982-09-24 1984-04-04 Becton Dickinson and Company Chemisch modifizierte Oberfläche zur Befestigung grosser Moleküle
JPS59216587A (ja) * 1983-05-25 1984-12-06 Nok Corp 生物活性物質の固定化方法
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EP0104608A1 (de) * 1982-09-24 1984-04-04 Becton Dickinson and Company Chemisch modifizierte Oberfläche zur Befestigung grosser Moleküle
JPS59216587A (ja) * 1983-05-25 1984-12-06 Nok Corp 生物活性物質の固定化方法
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Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1995034814A1 (en) * 1994-06-13 1995-12-21 Abbott Laboratories Plasma treatment of polymeric materials to enhance immobilization of analytes thereto
FR2847583A1 (fr) * 2002-11-27 2004-05-28 Centre Nat Rech Scient Procede d'oligomerisation de molecules, dispositif de mise en oeuvre dudit procede et utilisation
WO2004050745A1 (fr) * 2002-11-27 2004-06-17 Centre National De La Recherche Scientifique - Cnrs Procede d’oligomerisation de molecules, dispositif de mise en oeuvre dudit procede et utilisation
US7666478B2 (en) 2004-04-30 2010-02-23 Vlaamse Instelling Voor Technologisch Onderzoek (Vito) Biomolecule immobilisation using atmospheric plasma technology
US20120171354A1 (en) * 2010-12-13 2012-07-05 Enbio Limited Implantable medical devices
US8771782B2 (en) * 2010-12-13 2014-07-08 Enbio Limited Implantable medical devices

Also Published As

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JPH02131500A (ja) 1990-05-21
EP0351950A3 (de) 1990-03-28
US5306768A (en) 1994-04-26
US5028657A (en) 1991-07-02

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